EC Number   |
Recommended Name |
Application |
|---|
    1.13.11.37 | hydroxyquinol 1,2-dioxygenase |
degradation |
degradation of mixtures of phenolic compounds by Arthrobacter chlorophenolicus A6 |
| 1.13.11.37 | hydroxyquinol 1,2-dioxygenase |
degradation |
the highly purified Ar 1,2-HQD can be used as a key enzyme in the biodegradation of aromatic hydrocarbon contaminants |
| 1.13.11.39 | biphenyl-2,3-diol 1,2-dioxygenase |
degradation |
strain is able to degrade a solution containing benzene, toluene, ethylbenzene, and xylene at 7% NaCl (w/v) and pH 9 |
| 1.13.11.39 | biphenyl-2,3-diol 1,2-dioxygenase |
degradation |
the strain is able to completely degrade 280 microM of phenanthrene, 40% of 50 microM pyrene or 28% of 40 microM benzo[a]pyrene, each supplemented in M9 medium, within 7 days. The strain harbors genes which code for 2,3-dihydroxybiphenyl 1,2-dioxygenase (bphC), 4-nitrophenol 2-monooxygenase component B (npcB) as well as oxygenase component (nphA1), 4-hydroxybenzoate 3-monooxygenase (phbH), extradiol dioxygenase (edo), and naphthalene dioxygenase (ndo) |
| 1.13.11.39 | biphenyl-2,3-diol 1,2-dioxygenase |
degradation |
the strain is able to consume diphenyl ether and biphenyl from heat transfer fluid of thermo-solar plants (about 90% of total heat transfer fluid consumed after 1 day). The strain almost completely degrades 2,000 ppm heat transfer fluid after 5-day culture, and tolerates and grows in the presence of 150,000 ppm heat transfer fluid. When either biphenyl or diphenyl ether is used as sole carbon source, degradation is also effective |
| 1.13.11.55 | sulfur oxygenase/reductase |
degradation |
enzyme in the sulfur-oxidation pathway |
| 1.13.11.55 | sulfur oxygenase/reductase |
degradation |
initial enzyme in the sulfur-oxidation pathway |
| 1.13.11.56 | 1,2-dihydroxynaphthalene dioxygenase |
degradation |
the metabolic pathways of dibenzofuran and dibenzothiophene are controlled by naphthalene-degrading enzymes. Strain JB cannot grow on dibenzofuran or dibenzothiophen as the sole carbon source. 1,2-dihydroxynaphthalene dioxygenase may be responsible for the ring cleavage of 1,2-dihydroxydibenzofuran and 1,2-dihydroxydibenzothiophene to form 2-hydroxy-4-(3'-oxo-3'H-benzofuran-20-yliden)but-2-enoic acid and 4-[2-(3hydroxy)-thianaphthenyl]-2-oxo-3-butenoic acid |
| 1.13.11.87 | endo-cleaving rubber dioxygenase |
degradation |
enzyme exerts a synergistic effect on the efficiency of polyisoprene cleavage by rubber oxidase RoxA, EC 1.13.11.85 |
| 1.13.11.87 | endo-cleaving rubber dioxygenase |
degradation |
the enzyme has great potential for polyethylene and polypropylene degradation |
| 1.14.12.11 | toluene dioxygenase |
degradation |
stable isotopes could serve as a diagnostic for detecting aerobic biodegradation of TCE by toluene oxygenases at contaminated sites. There are no significant differences in fractionation among the enzymes toluene 3-monoxygenase, toluene 4-monooxygenase, and toluene 2,3-dioxygenase for compounds trichloroethene and cis-1,2-dichloroethene |
| 1.14.12.22 | carbazole 1,9a-dioxygenase |
degradation |
expression of genes CarAacd in dibenzothiophene degrader Rhodococcus erythropolis results in a strain capable of efficiently degrading dibenzothiophene and carbazole simultaneously. About 37% of the carbazole present, 0.8% by weight, is removed after treatment for 24 h.The recombinant strain can also degrade various alkylated derivatives of carbazole and dibenzothiophene in FS4800 crude oil by just a one-step bioprocess |
| 1.14.13.2 | 4-hydroxybenzoate 3-monooxygenase |
degradation |
in soil conditions, Phomopsis liquidambari effectively decomposes 99% of the available 4-hydroxybenzoic acid within 48 h. 4-Hydroxybenzoic acid hydroxylase activity is present in a high level early at 20 h, followed by 3,4-dihydroxybenzoic acid decarboxylase which reaches its highest relative activity at 24 h, and finally catechol 1,2-dioxygenase exhibits peak activity at 32 h |
| 1.14.13.7 | phenol 2-monooxygenase (NADPH) |
degradation |
phenol degradation, among kinetic parameters of growth, the maximum specific growth rate significantly affects the rate of contaminant degradation and is therefore an important parameter to characterise microbes in biological reatment systems |
| 1.14.13.20 | 2,4-dichlorophenol 6-monooxygenase |
degradation |
immobilized enzyme exhibits great potential for application in bioremediation |
| 1.14.13.25 | methane monooxygenase (soluble) |
degradation |
sMMO can be used for biodegradation of mixtures of chlorinated solvents, i.e., trichloroethylene, trans-dichloroethylene, and vinyl chloride. If the concentrations are increased to 0.1 mM, sMMO-expressing cells grow slower and degrade less of these pollutants in a shorter amount of time than pMMO |
| 1.14.13.50 | pentachlorophenol monooxygenase |
degradation |
pentachlorophenol is a chloroaromatic pesticide used to protect lumber, and an environmental pollutant, Sphingobium chlorophenolicum is a microorganism that can degrade the agent to 3-oxoadipate using 5 catalytic enzymes, pentachlorophenol 4-monooxygenase catalyzes the first and rate-limiting step |
| 1.14.13.227 | propane 2-monooxygenase |
degradation |
Rhodococcus sp. strain RHA1 can constitutively degrade N-nitrosodimethylamine. Activity toward this water contaminant is enhanced by approximately 500fold after growth on propane. Growth on propane elicits the upregulation of gene clusters associated with the oxidation of propane and the oxidation of substituted benzenes |
| 1.14.13.231 | tetracycline 11a-monooxygenase |
degradation |
addition of Escherichia coli overexpressing TetX to soil bacterial enrichment cultures along with varying levels of tetracycline affects community-wide tetracycline resistance levels. Soil microbial communities develop lower levels of tetracycline resistance upon exposure to 25 microg/ml of tetracycline when an Escherichia coli expressing TetX is present (6% of cultivable bacteria are resistant to 40 microg/ml tetracycline). In the absence of TetX activity, a similar tetracycline exposure selects for greater levels of resistant bacteria in the soil microbial community (90% of cultivable bacteria are resistant to 40 microg/ml tetracycline) |
| 1.14.13.243 | toluene 2-monooxygenase |
degradation |
coexpression of subunit TomA3 mutant V106A and an engineered epoxide hydrolase EchA from Agrobacterium radiobacter AD1, enhances the degradation of cis-dichloroethylene |
| 1.14.13.243 | toluene 2-monooxygenase |
degradation |
expression in Pseudomonas fluorescens for removal of trichloroethylene from soils. Closed microcosms containing the constitutive monooxygenase-expressing microorganism, soil, and wheat degrade an average of 63% of the initial trichloroethylene in 4 days (20.6 nmol of trichloroethylene/day and plant), compared to 9% of the initial trichloroethylene removed by microcosms containing wild-type Pseudomonas fluorescens 2-79 inoculated wheat, uninoculated wheat, or sterile soil |
| 1.14.13.244 | phenol 2-monooxygenase (NADH) |
degradation |
strain is able to degrade phenol at levels to 15 mM at a rate of 0.85 micromol/h |
| 1.14.15.3 | alkane 1-monooxygenase |
degradation |
formation of specific bacterial communities with reduced diversity after three week incubation of seawater with heptane, hexadecane, diesel fuel or crude oil. The isolates belong to well-known oil-degrading strains from the phyla Proteobacteria and Actinobacteria, whereas the genera Pseudomonas and Rhodococcus are represented with the biggest number of strains |
| 1.14.15.3 | alkane 1-monooxygenase |
degradation |
strain SJTD-1 efficiently mineralizes medium- and long-chain n-alkanes (C12-C30) as its sole carbon source within seven days, showing optimal growth on n-hexadecane, followed by n-octadecane, and n-eicosane. In 36 h, 500 mg/l of tetradecane, hexadecane, and octadecane are transformed completely; and 2 g/l n-hexadecane is degraded to undetectable levels within 72 h |
| 1.14.15.26 | toluene methyl-monooxygenase |
degradation |
presence of chlorinated toluenes induces expression of enzymes of the xylene degradation sequence. Conjugative transfer of the TOL plasmid from Pseudomonas putida strain PaW1 to Pseudomonas sp. strain B13 and Pseudomonas cepacia strain JH230 allows the isolation of hybrid strains capable of growing in the presence of 3-chloro-, 4-chloro- and 3,5-dichlorotoluene |
| 1.14.18.3 | methane monooxygenase (particulate) |
degradation |
pMMO can be used for biodegradation of mixtures of chlorinated solvents, i.e., trichloroethylene, trans-dichloroethylene, and vinyl chloride. If the concentrations are increased to 0.1 mM, pMMO-expressing cells grow faster and degrade more of these pollutants in a shorter amount of time than sMMO |
| 1.14.99.53 | lytic chitin monooxygenase |
degradation |
presence of lytic polysaccharide monooxygenase CBP21 facilitates the degradation of chitin substrates (colloidal chitin, beta-chitin, and alpha-chitin) by Chi92 |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
design of dockerin-fused lytic polysaccharide monooxygenases. The resulting chimeras exhibit activity levels on microcrystalline cellulose similar to that of the wild-type enzymes. The dockerin moieties of the chimeras are functional and specifically bind to their corresponding cohesin partner. The chimeric lytic polysaccharide monooxygenases are able to self-assemble in designer cellulosomes alongside an endo- and an exo-cellulase also converted to the cellulosomal mode. The resulting complexes show a 1.7fold increase in the release of soluble sugars from cellulose, compared with the free enzymes, and a 2.6fold enhancement compared with free cellulases without lytic polysaccharide monooxygenase enhancement |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
treatment with CelS2 reduces nonproductive binding of cellobiohydrolase onto cellulose surface |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
cellulose conversion by cellobiohydrolase Cel7A from Trichoderma longibrachiatum alone is enhanced from 46 to 54% by the addition of isoform AA9A. Conversion by a mixture of Cel7A, endoglucanase, and beta-glucosidase is increased from 79 to 87% using pretreated bacterial microcrystalline cellulose with AA9A for 72 h. Individual AA9A molecules exhibit intermittent random movement along, across, and penetrating into the ribbon-like microfibril structure of bacterial microcrystalline cellulose, concomitant with the release of a small amount of oxidized sugars and the splitting of large cellulose ribbons into fibrils with smaller diameters |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
in combination with endoglucanase and beta-glucosidase, Cel61A shows the ability to release more than 36% of the pretreated soy spent flake glucose |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
in combination with endoglucanase and beta-glucosidase, Pte6 shows the ability to release more than 36% of the pretreated soy spent flake glucose |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
in presence of a Trichoderma reesei CL847 cocktail composed of mainly cellulases and xylanases, a boost of glucose release from poplar and pine is observed upon addition of AA14B enzyme to the cocktail |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
in presence of a Trichoderma reesei CL847 cocktail composed of mainly cellulases and xylanases, a boost of glucose release from poplar and pine is observed upon addition of AA14B enzyme to the cocktail. Addition of AA14A to a GH11 xylanase increases the release of xylooligomers from birchwood cellulosic fibers by 40% |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
In the presence of an electron source, LPMO increases the activity of a commercial cellulase on filter paper, and the xylanase activity of xylanase Xyn10A on beechwood xylan. Mixtures of 60% Celluclast 1.5 L, 20% Xyn10A and 20% LPMO increase the total reducing sugar production from pretreated wheat straw by 54%, while the conversions of glucan to glucose and xylan to xylose are increased by 40 and 57%, respectively |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
lytic polysaccharide monooxygenase is able to cleave cellulose acetates with a degree of acetylation of up to 1.4 |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
oxidative activity of Cel61A displays a synergistic effect capable of boosting endoglucanase activity, and thereby substrate depolymerization of soy cellulose, by 27% |
| 1.14.99.54 | lytic cellulose monooxygenase (C1-hydroxylating) |
degradation |
the intrinsic physicochemical characteristics of Kraft pulp fibers (e.g. cellulose accessibility/degree of polymerization/crystallinity/charge) are positively enhanced by the synergistic cooperation of endoglucanase, LPMO and xylanase. LPMO addition results in the oxidative cleavage of the pulps, increasing the negative charge on the cellulose fibers, although gross fiber properties (fiber length, width and morphology) are relatively unchanged. This improves cellulose nanofibrilliation while stabilizing the nanofibril suspension, without sacrificing nanocellulose thermostability |
| 1.14.99.56 | lytic cellulose monooxygenase (C4-dehydrogenating) |
degradation |
in combination with endoglucanase and beta-glucosidase, Cel61A shows the ability to release more than 36% of the pretreated soy spent flake glucose |
| 1.14.99.56 | lytic cellulose monooxygenase (C4-dehydrogenating) |
degradation |
in combination with endoglucanase and beta-glucosidase, Pte6 shows the ability to release more than 36% of the pretreated soy spent flake glucose |
| 1.14.99.56 | lytic cellulose monooxygenase (C4-dehydrogenating) |
degradation |
lytic polysaccharide monooxygenase is able to cleave cellulose acetates with a degree of acetylation of up to 1.4 |
| 1.14.99.56 | lytic cellulose monooxygenase (C4-dehydrogenating) |
degradation |
oxidative activity of Cel61A displays a synergistic effect capable of boosting endoglucanase activity, and thereby substrate depolymerization of soy cellulose, by 27% |
| 1.14.99.56 | lytic cellulose monooxygenase (C4-dehydrogenating) |
degradation |
the intrinsic physicochemical characteristics of Kraft pulp fibers (e.g. cellulose accessibility/degree of polymerization/crystallinity/charge) are positively enhanced by the synergistic cooperation of endoglucanase, LPMO and xylanase. LPMO addition results in the oxidative cleavage of the pulps, increasing the negative charge on the cellulose fibers, although gross fiber properties (fiber length, width and morphology) are relatively unchanged. This improves cellulose nanofibrilliation while stabilizing the nanofibril suspension, without sacrificing nanocellulose thermostability |
| 1.20.4.1 | arsenate reductase (glutathione/glutaredoxin) |
degradation |
PvGrx5 has a role in regulating intracellular arsenite levels, by either directly or indirectly modulating the aquaglyceroporin |
| 1.97.1.1 | chlorate reductase |
degradation |
bacterial reduction of chlorate and perchlorate in water |
| 1.97.1.1 | chlorate reductase |
degradation |
(per)chlorate-reducing microorganisms are useful for bioremediation of soils and sediments |
| 1.97.1.1 | chlorate reductase |
degradation |
since the saturated hydrocarbon fraction is the most abundant in crude oil, its biodegradation is quantitatively most important in oil bioremediation |
| 2.1.1.8 | histamine N-methyltransferase |
degradation |
higher HMT activity seems to be linked to reduced histamine catabolism, percentage of catabolized histamine is not correlated to individual mannitol fluxes and appears to be independent of paracellular permeability |
| 2.1.1.41 | sterol 24-C-methyltransferase |
degradation |
active site of the yeast SMT has the necessary amino acids to generate products common to SMT catalysis of plants and protozoa, minor perturbations in the active site topography brought about by mutagenesis are sufficient to recognize new substrates |
| 2.1.1.137 | arsenite methyltransferase |
degradation |
Bacillus subtilis 168 expressing ArsM converts most of the inorganic As in the medium into dimethylarsenate and trimethylarsine oxide within 48 h and volatizes substantial amounts of dimethylarsine and trimethylarsine. The rate of As methylation and volatilization increases with temperature from 37 to 50°C. When inoculated into an As-contaminated organic manure composted at 50°C, the modified strain significantly enhances As volatilization |
| 2.1.1.142 | cycloartenol 24-C-methyltransferase |
degradation |
the amino acids of Region 1 provide a tight substrate orientation imposed by hydrophobic interactions between the sterol side chain and the SMT active site contacts and control the production and processing of the transmethylation pathways governed by the first and second C1-transfer activities |
| 2.1.2.1 | glycine hydroxymethyltransferase |
degradation |
essential for one-carbon metabolism |
| 2.3.1.12 | dihydrolipoyllysine-residue acetyltransferase |
degradation |
strain MM3 can grow on up to 250 microM pyrene in culture medium. With an initial cell density of 30000000 cells/ml, nearly 70% of 50 microM pyrene is degraded after 7 days of incubation. Nearly 20% increase in degradation of pyrene is observed with the use of 0.005% Tween 80. Dihydrolipoamide acetyltransferase accumulates during microalgal degradation of pyrene. The microalgal cells immobilized in calcium alginate completely degrade 50 microM of pyrene within 10 days in nonsterile soil slurry treated with 0.005% Tween 80 |
| 2.3.1.184 | acyl-homoserine-lactone synthase |
degradation |
a significant positive correlation is observed between isoform LasI expression and polycyclic aromatic hydrocarbon degradation. Expression of isoform LasI increases with increase in biofilm growth, while the expression of isoform RhlI decreases during log phase of biofilm growth. Degradation of phenanthrene and pyrene by Pseudomonas aeruginosa N6P6 is affected by biofilm growth and LasI expression. The respective phenanthrene degradation for 15, 24, 48, and 72 h old biofilm after 7 days is 21.5, 54.2, 85.6, and 85.7%. The corresponding pyrene degradation is 15, 18.28, 47.56, and 46.48%, respectively, after 7 days |
| 2.6.1.116 | 6-aminohexanoate aminotransferase |
degradation |
strain KI72 grows on a 6-aminohexanoate oligomer, a by-product of nylon-6 manufacturing, as a sole source of carbon and nitrogen |
| 2.7.2.2 | carbamate kinase |
degradation |
arginine is metabolized by the arginine deiminase pathway |
| 3.1.1.1 | carboxylesterase |
degradation |
use of enzyme in presence of oxime for detoxification of organophosphorous compounds |
| 3.1.1.1 | carboxylesterase |
degradation |
the enzyme can efficiently hydrolyze a wide range of synthetic pyrethroids including fenpropathrin, permethrin, cypermethrin, cyhalothrin, deltamethrin and bifenthrin, which makes it a potential candidate for the detoxification of pyrethroids for the purpose of biodegradation |
| 3.1.1.B12 | zearalenone hydrolase |
degradation |
effectively biological detoxification technology for ZEN degradation in agriculture and grain processing industry using enzyme ZHD. Biological detoxification of ZEN is more efficient, harmless, and specific compared to traditional methods |
| 3.1.1.B12 | zearalenone hydrolase |
degradation |
recombinant ZHD-P can be feasible for ZEN detoxification. The recombinant Escherichia coli cells expressing ZHD-P can be applied as a whole-cell biocatalyst for ZEN detoxification |
| 3.1.1.B12 | zearalenone hydrolase |
degradation |
zearalenone hydrolase (ZHD) is a lactone hydrolase with potential for the degradation of toxic and estrogenic zearalenone (ZEN). Importantly, ZHD does not damage cereal crops. ZHD catalyzes the cleavage of an ester bond in ZEN to form a non-toxic dihydroxyphenyl product with an open side chain with a subsequent loss of CO2, the product is non-estrogenic. Calculating the energy and electrostatic effects can provide a reference for the development of biodegradation technology in the field of environmental protection |
| 3.1.1.20 | tannase |
degradation |
TanSg1 is a tannase with potential industrial interest regarding the biodegradation of tannin waste or its bioconversion into biologically active products |
| 3.1.1.32 | phospholipase A1 |
degradation |
hydrolysis of nonpolar lipids, i.e. triacylglycerols, diacylglycerols and monoacylglycerols, when crude sunflower lecithin is treated with commercial product Lecitase VR Ultra. During the reaction, an acyl-migration phenomenon is observed. In 1 h of reaction the content of triacylglycerols decreases to 54%, while diacylglycerol and monoacylglycerol concentrations increase from 0.4 to 3.5 and from 1.9 to 6.5 g/100 g of crude lecithin, respectively. Along the reaction, different contents of glycerides can be achieved |
| 3.1.1.42 | chlorogenate hydrolase |
degradation |
use of yerba mate as source of chlorogenate and degradation by crude enzyme extract. Application to mass processing for a plant scale production of quinic acid |
| 3.1.1.60 | bis(2-ethylhexyl)phthalate esterase |
degradation |
di(2-ethylhexyl) phthalate, dibutyl phthalate, benzyl butyl phthalate and dipentyl phthalate can be almost completely degraded within four days in mineral salt medium under shaking conditions. 5.9% of the dimethyl phthalate and 42.9% of the diethyl phthalate present, are degraded under the same conditions. At temperatures of 10-50°C, strain B1811 is able to grow and utilize all the phthalate esters except for dimethylphthalate |
| 3.1.1.60 | bis(2-ethylhexyl)phthalate esterase |
degradation |
Fusarium culmorum degrades 95% of 1000 mg/l di(2-ethylhexyl) phthalate within 60 h of growth. Di(2-ethylhexyl) phthalate is fully metabolized wth butanediol as the final product |
| 3.1.1.72 | acetylxylan esterase |
degradation |
enzyme displays significant synergy with a xylanase, with a degree of synergy of 1.35 for the hydrolysis of delignified corn stover. Release of glucose is increased by 51% from delignified corn stover when 2 mg of a commercial cellulase is replaced by an equivalent amount of Axe |
| 3.1.1.72 | acetylxylan esterase |
degradation |
presence of the enzyme increases the activity of alpha-glucuronidases from families GH67 and GH115 on xylan by five and nine times, respectively |
| 3.1.1.72 | acetylxylan esterase |
degradation |
synergistic effect of AXE1 with xylanase on hemicellulose degradation. The amount of xylose released from acetylated birchwood xylan is increased by 1.4 fold when AXE1 is mixed with xylanase in a reaction cocktail |
| 3.1.1.73 | feruloyl esterase |
degradation |
capable of decolourising effluent from the paper industry, potential application in obtaining ferulic acid from agriculture waste materials produced by milling, brewing and sugar industries |
| 3.1.1.73 | feruloyl esterase |
degradation |
selective modification of xylans, degradation may be commercially important |
| 3.1.1.73 | feruloyl esterase |
degradation |
the esterase capable to release phenolic acids from intact polymers, degradation may be of interest for industries wishing to effect the controlled degradation of plant cell walls |
| 3.1.1.73 | feruloyl esterase |
degradation |
feruloyl esterase B is a tool for the release of phenolic compounds from agro-industrial by-products (coffe pulp, apple marc, wheat straw, sugar beet pulp and maite bran) |
| 3.1.1.73 | feruloyl esterase |
degradation |
feruloyl esterases A is a tool for the release of phenolic compounds from agro-industrial by-products (wheat straw, sugar beet pulp and maize bran) |
| 3.1.1.73 | feruloyl esterase |
degradation |
ferulic acid esterase activity in the enzymatic extracts of Aspergillus terreus grown on corn cob are higher than those after growth on vine trimming shoots. The enzymatic extracts produced on vine trimming shoots demonstrate a better performance for ferulic acid release from both corn cob (2.05 mg/g) and vine trimming shoots (0.19 mg/g), probably because of the higher xylanase/Fferulic acid esterase ratio determined in vine trimming extraxct |
| 3.1.1.73 | feruloyl esterase |
degradation |
maximum (76.8%) of total alkali-extractable ferulic acid is released from destarched wheat bran by the fungal enzyme system consisting of carboxymethyl cellulase, xylanase, beta-glucosidase, filter paper cellulase and ferulic acid esterase of Eupenicillium parvum 4-14 |
| 3.1.1.73 | feruloyl esterase |
degradation |
the endo-1,4-xylanase XynC11 from Penicillium funiculosum (CAC15487)and the feruloyl esterase CE1 from Clostridium thermocellum effectively break down hemicellulose from pretreated sugarcane bagasse (up to 65%), along with the production of xylooligosaccharides GH11 and CE1 can improve biomasssaccharification by cellulases. Treatment with these two enzymes followed by a commercial cellulase cocktail increases saccharification of pretreated lignocellulose by 24% |
| 3.1.1.73 | feruloyl esterase |
degradation |
the hydrolysis of corn stalk and corncob by xylanase from Aspergillus niger can be significantly improved in concert with recombinant FaeA |
| 3.1.1.73 | feruloyl esterase |
degradation |
addition of a crude enzyme supernatant from high xylanase producing actinomycete strain Kitasatospora sp. ID06-480 and ethyl ferulate producing actinomycete strain Nonomuraea sp. ID06-094 to sugarcane bagasse hydrolysis with low-level loading of commercial enzyme Cellic® CTec2 enhances both the released amount of glucose and reducing sugars. High conversion yield of glucose from cellulose at 60.5% can be achieved after 72 h of saccharification |
| 3.1.1.73 | feruloyl esterase |
degradation |
low doses of enzyme (120 microg/g substrate) increases glucose yields released from corn stover, wheat bran, corn cob, and cassava stillage residues by 68.8%, 38.6%, 15.6%, and 20.0%, respectively |
| 3.1.1.73 | feruloyl esterase |
degradation |
enzyme acts synergistically with commercial xylanase by improving the release of xylooligosaccharides from wheat arabinoxylan |
| 3.1.1.73 | feruloyl esterase |
degradation |
overexpression in Hypocrea jecorina leads to a high level of feruloyl esterase produced under solid-state fermentation. The recombinant fungal enzyme system can release 52.2% of total ferulic acids from destarched wheat bran |
| 3.1.1.73 | feruloyl esterase |
degradation |
overexpression in Hypocrea jecorina leads to a high level of feruloyl esterase produced under solid-state fermentation. The recombinant fungal enzyme system can release 62.9% of total ferulic acids from destarched wheat bran |
| 3.1.1.73 | feruloyl esterase |
degradation |
presence of enzyme enhances the quantity of ferulic acid from destarched wheat bran in presence of xylanase |
| 3.1.1.74 | cutinase |
degradation |
efficient degradation of n-butyl benzyl phthalate by enzyme, degradation of 60% of initial amount within 7.5 h. Major product is 1,3-isobenzofurandione |
| 3.1.1.74 | cutinase |
degradation |
enzyme degrades 60% of initial 500 mg/l malathion within 0.5 h, major degradation product is malathion diacid |
| 3.1.1.74 | cutinase |
degradation |
enzyme shows significant degradation of dipropyl phthalate to non-toxic 1,3-isobenzofurandione, with 70% degradation of initial 500 mg/l within 2.5 h |
| 3.1.1.74 | cutinase |
degradation |
biotechnological applications of cutinases for synthetic polyester degradation |
| 3.1.1.74 | cutinase |
degradation |
enzyme decreases the turbidity of poly(methyl acrylate) and poly(ethyl acrylate) dispersions |
| 3.1.1.74 | cutinase |
degradation |
enzyme decreases the turbidity of poly(methyl acrylate) and poly(ethyl acrylate) dispersions. It favors the hydrolysis of poly(ethyl acrylate) over poly(methyl acrylate) |
| 3.1.1.74 | cutinase |
degradation |
enzyme is able to modify the surface of the polycaprolactone and polyethylene terephthalate synthetic polyesters |
| 3.1.1.74 | cutinase |
degradation |
enzyme shows an ink removal efficiency of 78.4% on laser-printed paper and 81.3% on newspaper at 30°C |
| 3.1.1.74 | cutinase |
degradation |
fusion of enzyme to the class II hydrophobins HFB4 and HFB7 or the pseudo-class I hydrophobin HFB9b. Upon fusion to HFB4 or HFB7, the hydrolysis of polyethylene terephthalate is enhanced over16fold over the level with the free enzyme |
| 3.1.1.74 | cutinase |
degradation |
surface hydrolysis of poly(ethylene terephthalate) fabric using recombinant cutinase. The optimal parameters are 40°C, pH 8, and 1.92 mg enzyme loading per gram of fabric |
| 3.1.1.75 | poly(3-hydroxybutyrate) depolymerase |
degradation |
development of biodegradable plastics such as poly(3-hydroxybutyrate) or poly(3-hydroxybutyrate-co-3-hydroxyvalerate) |
| 3.1.1.75 | poly(3-hydroxybutyrate) depolymerase |
degradation |
About 8.58 g/l (R)-3-hydroxybutanoate is obtained after 8 h of incubation using extracellular PHB. The optimal conditions are 50°C and pH 8. Presence of CaCO3 increases (R)-3-hydroxybutanoate yields to 23.97 g/l by stabilizing the pH of the reaction system |
| 3.1.1.75 | poly(3-hydroxybutyrate) depolymerase |
degradation |
strain is able to degrade polyhydroxybutanoate film provided as sole carbon source, and readily degrades both polyhydroxybutanoate film and polyhydroxybutanoate particles in agar suspensions |
| 3.1.1.75 | poly(3-hydroxybutyrate) depolymerase |
degradation |
strain is able to degrade polyhydroxybutanoate film provided as sole carbon source, even at pH 3.3-3.7, and readily degrades both polyhydroxybutanoate film and polyhydroxybutanoate particles in agar suspensions |
| 3.1.1.75 | poly(3-hydroxybutyrate) depolymerase |
degradation |
the enzyme shows high percentage of degradation with poly(3-hydroxybutanoate) films with pH 9 and at 40°C |
| 3.1.1.75 | poly(3-hydroxybutyrate) depolymerase |
degradation |
the extra-cellular fraction of Escherichia coli expressing PhaZ exhibits a high poly(3-hydroxybutanoate) degradation rate. It takes 35 h to completely degrade oly(3-hydroxybutanoate) films, while Caldimonas manganoxidans takes 81 h. The coexpression of putative periplasmic substrate binding protein ORFCma further improves the PHB degradation. The enzyme is also able to degrade poly(lactic acid) polycaprolactone, and poly(butylene succinate-co-adipate) |
